ID   PRPC_SHEON              Reviewed;         375 AA.
AC   Q8EJW2;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=2-methylcitrate synthase {ECO:0000303|PubMed:14702315};
DE            Short=2-MCS {ECO:0000303|PubMed:14702315};
DE            Short=MCS {ECO:0000303|PubMed:14702315};
DE            EC=2.3.3.5 {ECO:0000250|UniProtKB:P31660};
DE   AltName: Full=Citrate synthase {ECO:0000250|UniProtKB:P31660};
DE            EC=2.3.3.16 {ECO:0000250|UniProtKB:P31660};
GN   Name=prpC; OrderedLocusNames=SO_0344;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
RN   [2]
RP   FUNCTION.
RC   STRAIN=MR-1;
RX   PubMed=14702315; DOI=10.1128/jb.186.2.454-462.2004;
RA   Grimek T.L., Escalante-Semerena J.C.;
RT   "The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new
RT   Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF
RT   function in vivo.";
RL   J. Bacteriol. 186:454-462(2004).
CC   -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC       via the tricarboxylic acid (TCA)(acetyl degradation route) and via the
CC       2-methylcitrate cycle II (propionate degradation route). Catalyzes the
CC       Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield
CC       2-methylcitrate (2-MC) and CoA (PubMed:14702315). Catalyzes the
CC       condensation of oxaloacetate with acetyl-CoA (By similarity).
CC       {ECO:0000250|UniProtKB:P31660, ECO:0000269|PubMed:14702315}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + oxaloacetate + propanoyl-CoA = (2S,3S)-2-methylcitrate +
CC         CoA + H(+); Xref=Rhea:RHEA:23780, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57392, ChEBI:CHEBI:58853; EC=2.3.3.5;
CC         Evidence={ECO:0000250|UniProtKB:P31660};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+);
CC         Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.3.16;
CC         Evidence={ECO:0000250|UniProtKB:P31660};
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000305}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 1/2. {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P31660}.
CC   -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR   EMBL; AE014299; AAN53429.1; -; Genomic_DNA.
DR   RefSeq; NP_715984.1; NC_004347.2.
DR   RefSeq; WP_011070709.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EJW2; -.
DR   SMR; Q8EJW2; -.
DR   STRING; 211586.SO_0344; -.
DR   PaxDb; Q8EJW2; -.
DR   KEGG; son:SO_0344; -.
DR   PATRIC; fig|211586.12.peg.334; -.
DR   eggNOG; COG0372; Bacteria.
DR   HOGENOM; CLU_025068_2_1_6; -.
DR   OMA; LTYCGYD; -.
DR   OrthoDB; 1412360at2; -.
DR   PhylomeDB; Q8EJW2; -.
DR   BioCyc; SONE211586:G1GMP-329-MON; -.
DR   UniPathway; UPA00223; UER00717.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0050440; F:2-methylcitrate synthase activity; IDA:UniProtKB.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IBA:GO_Central.
DR   GO; GO:0036440; F:citrate synthase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 1.10.230.10; -; 1.
DR   Gene3D; 1.10.580.10; -; 1.
DR   InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II.
DR   InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR   InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR   InterPro; IPR002020; Citrate_synthase.
DR   InterPro; IPR019810; Citrate_synthase_AS.
DR   InterPro; IPR024176; Citrate_synthase_bac-typ.
DR   InterPro; IPR036969; Citrate_synthase_sf.
DR   PANTHER; PTHR11739; PTHR11739; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PIRSF; PIRSF001369; Citrate_synth; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; SSF48256; 1.
DR   TIGRFAMs; TIGR01800; cit_synth_II; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..375
FT                   /note="2-methylcitrate synthase"
FT                   /id="PRO_0000432971"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000250|UniProtKB:O34002"
FT   ACT_SITE        261
FT                   /evidence="ECO:0000250|UniProtKB:O34002"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000250|UniProtKB:O34002"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT   BINDING         255..259
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:O34002"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT   BINDING         337
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT   BINDING         356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
SQ   SEQUENCE   375 AA;  41431 MW;  C41B9ED9842F7986 CRC64;
     MSDAKKLTGA GLRGQSAGET ALSTVGVSGS GLTYRGYDVK DLAENATFEE VAYLILYGEL
     PTTAQLAAYK TKLKGMRGLP QALKEVLERI PADAHPMDVM RTGCSMLGNL EAEHSFSEQS
     QIADRLLAAF PSIICYWYRF SHDGVRIDTE TDDDQIGAHF LHLLHGKAPS ALHTKVMDVS
     LILYAEHEFN ASTFTARVCA STLSDMHSCV TGAIGSLRGP LHGGANEAAM ELIQDMKDEA
     DARDVLMGKL ERKEKIMGFG HAIYRDSDPR NAIIKEWSEK LAADYGDDRL YRVSVACEAL
     MWEQKKLFCN ADFFHASAYH FMGIPTKLFT PIFVCSRVTG WTAHVMEQRS NNRIIRPSAD
     YVGVSPRKVI PIANR